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Volumn 90, Issue 6, 2004, Pages 1489-1499

Acetylcholinesterase inhibitors increase ADAM10 activity by promoting its trafficking in neuroblastoma cell lines

Author keywords

Acetylcholinesterase; ADAM 10; Alzheimer's disease; Donepezil; Neuroblastoma; Trafficking

Indexed keywords

ALPHA SECRETASE; AMYLOID PRECURSOR PROTEIN; CHOLINESTERASE INHIBITOR; DONEPEZIL; METALLOPROTEINASE; METALLOPROTEINASE ADAM 10; UNCLASSIFIED DRUG;

EID: 4544239545     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2004.02680.x     Document Type: Article
Times cited : (128)

References (59)
  • 1
    • 0038238122 scopus 로고    scopus 로고
    • Effect of a new derivative of retinoic acid on proliferation and differentiation in human neuroblastoma cells
    • Bartolini G., Orlandi M., Ammar K., Magrini E., Ferreri A. M. and Rocchi P. (2003) Effect of a new derivative of retinoic acid on proliferation and differentiation in human neuroblastoma cells. Anticancer. Res. 23, 1495-1499.
    • (2003) Anticancer. Res. , vol.23 , pp. 1495-1499
    • Bartolini, G.1    Orlandi, M.2    Ammar, K.3    Magrini, E.4    Ferreri, A.M.5    Rocchi, P.6
  • 2
    • 0037422539 scopus 로고    scopus 로고
    • Interaction of 'readthrough' acetylcholinesterase with RACK1 and PKCbeta II correlates with intensified fear-induced conflict behavior
    • Birikh K. R., Sklan E. H., Shoham S. and Soreq H. (2003) Interaction of 'readthrough' acetylcholinesterase with RACK1 and PKCbeta II correlates with intensified fear-induced conflict behavior. Proc. Natl Acad. Sci. USA 100, 283-288.
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 283-288
    • Birikh, K.R.1    Sklan, E.H.2    Shoham, S.3    Soreq, H.4
  • 3
    • 0035853821 scopus 로고    scopus 로고
    • A splice variant of β-secretase deficient in the amyloidogenic processing of the amyloid precursor protein
    • Bodendorf U., Fischer F., Bodian D., Multhaup G. and Paganetti P. (2001) A splice variant of β-secretase deficient in the amyloidogenic processing of the amyloid precursor protein. J. Biol. Chem. 276, 12019-12023.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12019-12023
    • Bodendorf, U.1    Fischer, F.2    Bodian, D.3    Multhaup, G.4    Paganetti, P.5
  • 4
    • 0035107233 scopus 로고    scopus 로고
    • Amyloid precursor protein in platelets of patients with Alzheimer disease: Effect of acetylcholinesterase inhibitor treatment
    • Borroni B., Colciaghi F., Pastorino L. et al. (2001) Amyloid precursor protein in platelets of patients with Alzheimer disease: effect of acetylcholinesterase inhibitor treatment. Arch. Neurol. 58, 442-446.
    • (2001) Arch. Neurol. , vol.58 , pp. 442-446
    • Borroni, B.1    Colciaghi, F.2    Pastorino, L.3
  • 6
    • 0028207004 scopus 로고
    • Calcium regulates processing of the Alzheimer's amyloid protein precursor in a protein kinase C-independent manner
    • Buxbaum J. D., Ruefly A. A., Parker C. A., Cypress A. M. and Greengard P. (1994) Calcium regulates processing of the Alzheimer's amyloid protein precursor in a protein kinase C-independent manner. Proc. Natl Acad. Sci. USA 91, 4489-4493.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4489-4493
    • Buxbaum, J.D.1    Ruefly, A.A.2    Parker, C.A.3    Cypress, A.M.4    Greengard, P.5
  • 7
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha-converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid precursor protein
    • Buxbaum J. D., Liu K. N., Luo X., Stocking K. L., Peschon J. J., Johnson R. S., Castner B. J., Cerretti D. P. and Black R. A. (1998) Evidence that tumor necrosis factor alpha-converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid precursor protein. J. Biol. Chem. 273, 27765-27767.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, X.3    Stocking, K.L.4    Peschon, J.J.5    Johnson, R.S.6    Castner, B.J.7    Cerretti, D.P.8    Black, R.A.9
  • 9
    • 0026539070 scopus 로고
    • Conformational analysis and molecular shape comparisons of a series of indanone-benzylpiperidine inhibitors of acetylcholinesterase
    • Cardozo M. G., Kawani T., Iimura Y., Sugimoto H., Yamanishi Y. and Hopfinger A. J. (1992) Conformational analysis and molecular shape comparisons of a series of indanone-benzylpiperidine inhibitors of acetylcholinesterase. J. Med. Chem. 35, 590-601.
    • (1992) J. Med. Chem. , vol.35 , pp. 590-601
    • Cardozo, M.G.1    Kawani, T.2    Iimura, Y.3    Sugimoto, H.4    Yamanishi, Y.5    Hopfinger, A.J.6
  • 10
    • 0035896466 scopus 로고    scopus 로고
    • Differential increase in cerebrospinal fluid-acetylcholinesterase after treatment with acetylcholinesterase inhibitors in patients with Alzheimer's disease
    • Davidsson P., Blennow K., Andreasen N., Eriksson B., Minthon L. and Hesse C. (2001) Differential increase in cerebrospinal fluid-acetylcholinesterase after treatment with acetylcholinesterase inhibitors in patients with Alzheimer's disease. Neurosci. Lett. 300, 157-160.
    • (2001) Neurosci. Lett. , vol.300 , pp. 157-160
    • Davidsson, P.1    Blennow, K.2    Andreasen, N.3    Eriksson, B.4    Minthon, L.5    Hesse, C.6
  • 11
    • 0032489322 scopus 로고    scopus 로고
    • Effects of the M1 agonist xanomeline on processing of human beta-amyloid precursor protein (FAD, Swedish mutant) transfected into Chinese hamster ovary-m1 cells
    • DeLapp N., Wu S., Belagaje R. et al. (1998) Effects of the M1 agonist xanomeline on processing of human beta-amyloid precursor protein (FAD, Swedish mutant) transfected into Chinese hamster ovary-m1 cells. Biochem. Biophys. Res. Commun. 244, 156-160.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 156-160
    • DeLapp, N.1    Wu, S.2    Belagaje, R.3
  • 14
    • 0037716445 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation
    • Endres K., Anders A., Kojro E., Gilbert S., Fahrenholz F. and Postina R. (2003) Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation. Eur. J. Biochem. 270, 2386-2393.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2386-2393
    • Endres, K.1    Anders, A.2    Kojro, E.3    Gilbert, S.4    Fahrenholz, F.5    Postina, R.6
  • 15
    • 0242267132 scopus 로고    scopus 로고
    • Proteolytic processing of the Alzheimer's disease amyloid precursor protein in brain and platelets
    • Evin G., Zhu A., Holsinger R. M., Masters C. L. and Li Q. X. (2003) Proteolytic processing of the Alzheimer's disease amyloid precursor protein in brain and platelets. J. Neurosci. Res. 74, 386-392.
    • (2003) J. Neurosci. Res. , vol.74 , pp. 386-392
    • Evin, G.1    Zhu, A.2    Holsinger, R.M.3    Masters, C.L.4    Li, Q.X.5
  • 16
    • 0029670364 scopus 로고    scopus 로고
    • Tetrameric (G4) acetylcholinesterase: Structure, localization, and physiological regulation
    • Fernandez H. L., Moreno R. D. and Inestrosa N. C. (1996) Tetrameric (G4) acetylcholinesterase: structure, localization, and physiological regulation. J. Neurochem. 66, 1335-1346.
    • (1996) J. Neurochem. , vol.66 , pp. 1335-1346
    • Fernandez, H.L.1    Moreno, R.D.2    Inestrosa, N.C.3
  • 17
    • 0025336841 scopus 로고
    • On the involvement of multiple muscarinic receptor subtypes in the activation of phosphoinositide metabolism in rat cerebral cortex
    • Forray C. and el-Fakahany E. E. (1990) On the involvement of multiple muscarinic receptor subtypes in the activation of phosphoinositide metabolism in rat cerebral cortex. Mol. Pharmacol. 37, 893-902.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 893-902
    • Forray, C.1    El-Fakahany, E.E.2
  • 18
    • 0035123732 scopus 로고    scopus 로고
    • Do cholinesterase inhibitors have disease-modifying effects in Alzheimer's disease?
    • Giacobini E. (2001) Do cholinesterase inhibitors have disease-modifying effects in Alzheimer's disease? CNS Drugs 15, 85-91.
    • (2001) CNS Drugs , vol.15 , pp. 85-91
    • Giacobini, E.1
  • 19
    • 0029983531 scopus 로고    scopus 로고
    • The effect of cholinesterase inhibitors on the secretion of APPS from rat brain cortex
    • Giacobini E., Mori F. and Lai C. C. (1996) The effect of cholinesterase inhibitors on the secretion of APPS from rat brain cortex. Ann. NY Acad. Sci. 777, 393-398.
    • (1996) Ann. NY Acad. Sci. , vol.777 , pp. 393-398
    • Giacobini, E.1    Mori, F.2    Lai, C.C.3
  • 20
    • 0021256895 scopus 로고
    • Alzheimer disease: Initial report of the purification and characterization of novel cerebrovascular amyloid protein
    • Glenner G. G. and Wong C. W. (1984) Alzheimer disease: initial report of the purification and characterization of novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Comm. 120, 885-890.
    • (1984) Biochem. Biophys. Res. Comm. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 21
    • 0036065158 scopus 로고    scopus 로고
    • Muscarinic receptor-mediated phosphorylation of cyclic AMP response element binding protein in human neuroblastoma cells
    • Greenwood M. and Dragunow M. (2002) Muscarinic receptor-mediated phosphorylation of cyclic AMP response element binding protein in human neuroblastoma cells. J. Neurochem. 82, 389-397.
    • (2002) J. Neurochem. , vol.82 , pp. 389-397
    • Greenwood, M.1    Dragunow, M.2
  • 23
    • 0343570105 scopus 로고    scopus 로고
    • Modulation of beta-amyloid precursor protein processing and tau phosphorylation by acetylcholin receptors
    • Hellström-Lindahl E. (2000) Modulation of beta-amyloid precursor protein processing and tau phosphorylation by acetylcholin receptors. Eur. J. Pharmacol. 393, 255-263.
    • (2000) Eur. J. Pharmacol. , vol.393 , pp. 255-263
    • Hellström-Lindahl, E.1
  • 26
    • 0037013209 scopus 로고    scopus 로고
    • Beta-secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain
    • Huse J. T., Liu K., Pijak D. S., Carlin D., Lee V. M.-Y. and Doms R. W. (2002) beta-Secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain. J. Biol. Chem. 277, 16278-16284.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16278-16284
    • Huse, J.T.1    Liu, K.2    Pijak, D.S.3    Carlin, D.4    Lee, V.M.-Y.5    Doms, R.W.6
  • 27
    • 0032574973 scopus 로고    scopus 로고
    • Acute stress facilitates long-lasting changes in cholinergic gene expression
    • Kaufer D., Friedman A., Seidman S. and Soreq H. (1998) Acute stress facilitates long-lasting changes in cholinergic gene expression. Nature 393, 373-377.
    • (1998) Nature , vol.393 , pp. 373-377
    • Kaufer, D.1    Friedman, A.2    Seidman, S.3    Soreq, H.4
  • 28
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase
    • Kojro E., Giml G., Lammich S., Marz W. and Fahrenholz F. (2001) Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase. Proc. Natl Acad. Sci. USA 98, 5815-5820.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 5815-5820
    • Kojro, E.1    Giml, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 29
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endocytic pathway
    • Koo E. H. and Squazzo S. (1994) Evidence that production and release of amyloid beta-protein involves the endocytic pathway. J. Biol. Chem. 269, 173-186.
    • (1994) J. Biol. Chem. , vol.269 , pp. 173-186
    • Koo, E.H.1    Squazzo, S.2
  • 30
    • 0032931885 scopus 로고    scopus 로고
    • Cholinesterase inhibitors: A therapeutic strategy for Alzheimer disease
    • Krall W. J., Sramek J. J. and Cutler N. R. (1999) Cholinesterase inhibitors: a therapeutic strategy for Alzheimer disease. Ann. Pharmacotherapy 33, 441-450.
    • (1999) Ann. Pharmacotherapy , vol.33 , pp. 441-450
    • Krall, W.J.1    Sramek, J.J.2    Cutler, N.R.3
  • 31
    • 0142258009 scopus 로고    scopus 로고
    • Involvement of endogenous ceramide in the inhibition of telomerase activity and induction of morphologic differentiation in response to all-trans-retinoic acid in human neuroblastoma cells
    • Kraveka J. M., Li L., Bielawski J., Obeid L. M. and Ogretmen B. (2003) Involvement of endogenous ceramide in the inhibition of telomerase activity and induction of morphologic differentiation in response to all-trans-retinoic acid in human neuroblastoma cells. Arch. Biochem. Biophys. 419, 110-119.
    • (2003) Arch. Biochem. Biophys. , vol.419 , pp. 110-119
    • Kraveka, J.M.1    Li, L.2    Bielawski, J.3    Obeid, L.M.4    Ogretmen, B.5
  • 32
    • 0028197477 scopus 로고
    • Tacrine alters the secretion of the beta-amyloid precursor protein in cell lines
    • Lahiri D. K., Lewis S. and Farlow M. R. (1994) Tacrine alters the secretion of the beta-amyloid precursor protein in cell lines. J. Neurosci. Res. 37, 777-787.
    • (1994) J. Neurosci. Res. , vol.37 , pp. 777-787
    • Lahiri, D.K.1    Lewis, S.2    Farlow, M.R.3
  • 33
    • 0032569990 scopus 로고    scopus 로고
    • The secretion of amyloid beta-peptides is inhibited in the tacrine-treated human neuroblastoma cells
    • Lahiri D. K., Farlow M. R. and Sambamurti K. (1998) The secretion of amyloid beta-peptides is inhibited in the tacrine-treated human neuroblastoma cells. Brain Res. Mol. Brain Res. 20, 131-140.
    • (1998) Brain Res. Mol. Brain Res. , vol.20 , pp. 131-140
    • Lahiri, D.K.1    Farlow, M.R.2    Sambamurti, K.3
  • 34
    • 0034489269 scopus 로고    scopus 로고
    • Cholinesterase inhibitors, beta-amyloid precursor protein and amyloid beta-peptides in Alzheimer's disease
    • Lahiri D. K., Farlow M. R., Hintz N., Utsuki T. and Greig N. H. (2000) Cholinesterase inhibitors, beta-amyloid precursor protein and amyloid beta-peptides in Alzheimer's disease. Acta Neurol. Scand. Suppl. 176, 60-67.
    • (2000) Acta Neurol. Scand. Suppl. , vol.176 , pp. 60-67
    • Lahiri, D.K.1    Farlow, M.R.2    Hintz, N.3    Utsuki, T.4    Greig, N.H.5
  • 36
    • 0032523039 scopus 로고    scopus 로고
    • Protein kinase C activation increases release of secreted amyloid precursor protein without decreasing Abeta production in human primary neuron cultures
    • LeBlanc A. C., Koutroumanis M. and Goodyer C. G. (1998) Protein kinase C activation increases release of secreted amyloid precursor protein without decreasing Abeta production in human primary neuron cultures. J. Neurosci. 18, 2907-2913.
    • (1998) J. Neurosci. , vol.18 , pp. 2907-2913
    • LeBlanc, A.C.1    Koutroumanis, M.2    Goodyer, C.G.3
  • 38
    • 0032960305 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein cleavage
    • Mills J. and Reiner P. B. (1999) Regulation of amyloid precursor protein cleavage. J. Neurochem. 72, 443-460.
    • (1999) J. Neurochem. , vol.72 , pp. 443-460
    • Mills, J.1    Reiner, P.B.2
  • 39
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch R. M., Slack B. E., Wurtman T. J. and Growdon J. H. (1992) Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 258, 304-307.
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, T.J.3    Growdon, J.H.4
  • 41
    • 0034644836 scopus 로고    scopus 로고
    • Regulation of APP cleavage by alpha-, beta- and gamma-secretases
    • Nunan J. and Small D. H. (2000) Regulation of APP cleavage by alpha-, beta- and gamma-secretases. FEBS Lett. 483, 6-10.
    • (2000) FEBS Lett. , vol.483 , pp. 6-10
    • Nunan, J.1    Small, D.H.2
  • 42
    • 0025264201 scopus 로고
    • The Alzheimer amyloid precursor protein: Identification of a stable intermediate in the biosynthetic/degradative pathway
    • Oltersdorf T. (1990) The Alzheimer amyloid precursor protein: identification of a stable intermediate in the biosynthetic/degradative pathway. J. Biol. Chem. 265, 4492-4497.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4492-4497
    • Oltersdorf, T.1
  • 43
    • 0042970733 scopus 로고    scopus 로고
    • Role of acetylcholinesterase inhibitors in the metabolism of amyloid precursor protein
    • Pakaski M. and Kasa P. (2003) Role of acetylcholinesterase inhibitors in the metabolism of amyloid precursor protein. Curr. Drug Target CNS Neurl. Disord. 3, 163-171.
    • (2003) Curr. Drug Target CNS Neurl. Disord. , vol.3 , pp. 163-171
    • Pakaski, M.1    Kasa, P.2
  • 44
    • 0035196471 scopus 로고    scopus 로고
    • Reversible and irreversible acetylcholinesterase inhibitors cause changes in neuronal amyloid precursor protein processing and protein kinase C level in vitro
    • Pakaski M., Rakonczay Z. and Kasa P. (2001) Reversible and irreversible acetylcholinesterase inhibitors cause changes in neuronal amyloid precursor protein processing and protein kinase C level in vitro. Neurochem. Int. 38, 219-226.
    • (2001) Neurochem. Int. , vol.38 , pp. 219-226
    • Pakaski, M.1    Rakonczay, Z.2    Kasa, P.3
  • 45
    • 0032502033 scopus 로고    scopus 로고
    • Alzheimer's amyloid precursor protein alpha-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: Similarities to the angiotensin converting enzyme secretase
    • Parvathy S., Hussain I., Karran E. H., Turner A. J. and Hooper N. M. (1998) Alzheimer's amyloid precursor protein alpha-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: similarities to the angiotensin converting enzyme secretase. Biochemistry 37, 1680-1685.
    • (1998) Biochemistry , vol.37 , pp. 1680-1685
    • Parvathy, S.1    Hussain, I.2    Karran, E.H.3    Turner, A.J.4    Hooper, N.M.5
  • 46
    • 0037008737 scopus 로고    scopus 로고
    • Dynamic change of neural cell adhesion molecule polysialylation on human neuroblastoma (IMR-32) and rat pheochromocytoma (PC-12) cells during growth and differentiation
    • Poongodi G. L., Suresh N., Gopinath S. C., Chang T., Inoue S. and Inoue Y. (2002) Dynamic change of neural cell adhesion molecule polysialylation on human neuroblastoma (IMR-32) and rat pheochromocytoma (PC-12) cells during growth and differentiation. J. Biol. Chem. 277, 28200-28211.
    • (2002) J. Biol. Chem. , vol.277 , pp. 28200-28211
    • Poongodi, G.L.1    Suresh, N.2    Gopinath, S.C.3    Chang, T.4    Inoue, S.5    Inoue, Y.6
  • 47
    • 0242459186 scopus 로고    scopus 로고
    • Simultaneous changes in secretory amyloid precursor protein and beta-amyloid peptide release from rat hippocampus by activation of muscarinic receptors
    • Qiu Y., Wu X. J. and Chen H. Z. (2003) Simultaneous changes in secretory amyloid precursor protein and beta-amyloid peptide release from rat hippocampus by activation of muscarinic receptors. Neurosci. Lett. 352, 41-44.
    • (2003) Neurosci. Lett. , vol.352 , pp. 41-44
    • Qiu, Y.1    Wu, X.J.2    Chen, H.Z.3
  • 48
    • 0033049442 scopus 로고    scopus 로고
    • Activity of alpha-secretase as the common final effector of protein Kinase C-dependent and -independent modulation of amyloid precursor protein metabolism
    • Racchi M., Solano D. C., Sironi M. and Govoni S. (1999) Activity of alpha-secretase as the common final effector of protein Kinase C-dependent and -independent modulation of amyloid precursor protein metabolism. J. Neurochem. 72, 2464-2470.
    • (1999) J. Neurochem. , vol.72 , pp. 2464-2470
    • Racchi, M.1    Solano, D.C.2    Sironi, M.3    Govoni, S.4
  • 49
    • 0034885166 scopus 로고    scopus 로고
    • Short and long-term effect of acetylcholinesterase inhibitors on the expression and metabolism of the amyloid precursor protein
    • Racchi M., Sironi M., Caprera A., Konig G. and Gorono S. (2001) Short and long-term effect of acetylcholinesterase inhibitors on the expression and metabolism of the amyloid precursor protein. Mol. Psychiatry 6, 520-528.
    • (2001) Mol. Psychiatry , vol.6 , pp. 520-528
    • Racchi, M.1    Sironi, M.2    Caprera, A.3    Konig, G.4    Gorono, S.5
  • 50
    • 0032311033 scopus 로고    scopus 로고
    • Long-term cognitive benefit from galantamine in Alzheimer's disease
    • Rainer M. and Mucke H. A. M. (1999) Long-term cognitive benefit from galantamine in Alzheimer's disease. Int. J. Ger. Psy. 1, 197-201.
    • (1999) Int. J. Ger. Psy. , vol.1 , pp. 197-201
    • Rainer, M.1    Mucke, H.A.M.2
  • 51
    • 0032507788 scopus 로고    scopus 로고
    • Donepezil improves cognition and global function in Alzheimer's disease: A 15-week double blind placebo-controlled study
    • Rogers S. L., Doody R. S., Mohs R. C. and Friedhoff L. T. (1998) donepezil improves cognition and global function in Alzheimer's disease: a 15-week double blind placebo-controlled study. Arch. Int. Med. 158, 1021-1031.
    • (1998) Arch. Int. Med. , vol.158 , pp. 1021-1031
    • Rogers, S.L.1    Doody, R.S.2    Mohs, R.C.3    Friedhoff, L.T.4
  • 52
    • 0025753852 scopus 로고
    • The molecular pathology of Alzheimer's disease
    • Selkoe D. J. (1991) The molecular pathology of Alzheimer's disease. Neuron 6, 487-498.
    • (1991) Neuron , vol.6 , pp. 487-498
    • Selkoe, D.J.1
  • 53
    • 0033613129 scopus 로고    scopus 로고
    • Cellular mechanisms of beta-amyloid production and secretion
    • Sinha S. and Lieberburg I. (1999) Cellular mechanisms of beta-amyloid production and secretion. Proc. Natl Acad. Sci. USA 96, 11049-11053.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 11049-11053
    • Sinha, S.1    Lieberburg, I.2
  • 54
    • 0035424693 scopus 로고    scopus 로고
    • Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme
    • Slack B. E., Ma L. K. and Seah C. C. (2001) Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme. Biochem. J. 357, 787-794.
    • (2001) Biochem. J. , vol.357 , pp. 787-794
    • Slack, B.E.1    Ma, L.K.2    Seah, C.C.3
  • 55
    • 0035320772 scopus 로고    scopus 로고
    • Acetylcholinesterase - New roles for an old actor
    • Soreq H. and Seidman S. (2001) Acetylcholinesterase - new roles for an old actor. Nat. Rev. Neurosci. 2, 294-302.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 294-302
    • Soreq, H.1    Seidman, S.2
  • 56
    • 0037425565 scopus 로고    scopus 로고
    • Efficacy of cholinesterase inhibitors in the treatment of neuropsychiatric symptoms and functional impairment in Alzheimer disease: A meta-analysis
    • Trinh N. H., Hoblyn J., Mohanty S. and Yaffe K. (2003) Efficacy of cholinesterase inhibitors in the treatment of neuropsychiatric symptoms and functional impairment in Alzheimer disease: a meta-analysis. JAMA 289, 210-216.
    • (2003) JAMA , vol.289 , pp. 210-216
    • Trinh, N.H.1    Hoblyn, J.2    Mohanty, S.3    Yaffe, K.4
  • 58
    • 0028859466 scopus 로고
    • Regulated formation of golgi secretory vesicles containing Alzheimer beta-amyloid precursor protein
    • Xu H., Greengard P. and Gandy S. (1994) Regulated formation of golgi secretory vesicles containing Alzheimer beta-amyloid precursor protein. J. Biol. Chem. 270, 23243-23245.
    • (1994) J. Biol. Chem. , vol.270 , pp. 23243-23245
    • Xu, H.1    Greengard, P.2    Gandy, S.3
  • 59
    • 0029896354 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • Yankner B. A. (1996) Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 16, 921-932.
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.